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The KgPs showed micromolar affinities with A\u03b21\u201342 and abolished its sigmoidal amyloidogenic transition, resulting in abrogation of fibrillogenesis. Comprehensive assessment using dynamic light scattering (DLS), atomic force microscopy (AFM) and Fourier-transform infrared (FTIR) spectroscopy showed that KgPs induced the formation of off-pathway oligomers comparatively larger than the native A\u03b21\u201342 oligomers but with a significantly reduced cross-\u03b2 signature. These off-pathway oligomers exhibited low immunoreactivity against oligomer-specific (A11) and fibril-specific (OC) antibodies and rescued neuronal cells from A\u03b21\u201342 oligomer toxicity as well as neuronal apoptosis. Structural analysis using molecular docking and molecular dynamics (MD) simulations showed two preferred KgP binding sites (Lys16\u2013Phe20 and Leu28\u2013Val39) on the NMR ensembles of monomeric and fibrillar A\u03b21\u201342, indicating an interruption of crucial hydrophobic and aromatic interactions. Overall, our results demonstrate a new approach for designing potential anti-amyloid molecules that could pave way for developing effective therapeutics against AD and other amyloid diseases.<\/jats:p>","DOI":"10.1042\/bcj20190183","type":"journal-article","created":{"date-parts":[[2019,5,28]],"date-time":"2019-05-28T21:15:32Z","timestamp":1559078132000},"page":"1817-1841","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Specific keratinase derived designer peptides potently inhibit A<i>\u03b2<\/i> aggregation resulting in reduced neuronal toxicity and apoptosis"],"prefix":"10.1042","volume":"476","author":[{"given":"Rinky","family":"Rajput","sequence":"first","affiliation":[{"name":"School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Balasubramani","family":"G L","sequence":"additional","affiliation":[{"name":"School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ankit","family":"Srivastava","sequence":"additional","affiliation":[{"name":"Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, New Delhi 110016, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Divya","family":"Wahi","sequence":"additional","affiliation":[{"name":"School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nidhi","family":"Shrivastava","sequence":"additional","affiliation":[{"name":"School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5786-3144","authenticated-orcid":false,"given":"Bishwajit","family":"Kundu","sequence":"additional","affiliation":[{"name":"Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, New Delhi 110016, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3296-7860","authenticated-orcid":false,"given":"Abhinav","family":"Grover","sequence":"additional","affiliation":[{"name":"School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2019,6,28]]},"reference":[{"key":"2021112217583105600_BCJ-2019-0183C1","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1016\/S0304-3940(96)13147-5","article-title":"Laminin inhibits amyloid-\u03b2-peptide fibrillation","volume":"218","year":"1996","journal-title":"Neurosci. 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